Disease relevance of CRSP2

• DRIP150 coactivates ligand-dependent ERalpha-mediated transactivation in ZR-75 and MDA-MB-231 breast cancer cells transfected with a (luciferase) reporter construct (pERE3) regulated by three tandem estrogen-responsive elements [1].

High impact information on CRSP2

• In yeast and mammalian cells, TSG101 represses whereas DRIP150 enhances GR AF-1-mediated transactivation [2].
• We further show that the association between the activation domain of SREBP-1 and mediator is through aa 500 to 824 of DRIP150 [3].
• In the present study, we show that ISGF3-mediated transcription is dependent on STAT2 interactions with DRIP150, a subunit of the multimeric Mediator coactivator complex [4].
• Vitamin D receptor-interacting protein 150 (DRIP150) has been identified as part of mediator-like complexes that enhance transcriptional activation of the estrogen receptor (ER) and other nuclear receptors (NRs) [1].
• By using a squelching assay and specific amino acid point mutations within each alpha-helix, the NIFSEVRVYN (795-804) region was identified as the critical sequence required for the activity of DRIP150 [1].

Biological context of CRSP2

• However, due to its expression in different tissues and its contribution to transcriptional regulation, CRSP2 may be a candidate for other diseases that map to this region of the X chromosome [5].
• In the course of our search for the gene responsible for X-linked cone-rod dystrophy (COD1), we constructed a physical map and contig (encompassing the region between DXS556 and DXS228), and identified sequences showing homologies to the expressed sequence tags (ESTs) that matched CRSP2 (EXLM1) transcript [5].
• Orf1 has sequence similarities to the B2 repetitive element and human CXORF4 (formerly called EXLM1), which escapes X inactivation [6].
• The conserved amino acid sequences of RGR from various mammals can be compared to the amino acid sequence motif of G protein-coupled receptors [7].
• Three of the markers (tel-OTC, TRAP170 and (ps)ALDH2- cen) located on the short arm of ECAX and EZHX were found inverted on the long arm of EASX, along with the transposition of the centromere [8].

Anatomical context of CRSP2

• One of the genes matched a known gene, but the other, termed EXLM1, is novel and is predominantly expressed in cultured lymphocytes and skeletal muscle [9].
• CONCLUSIONS: Using a Lentivirus-derived gene delivery system, we were able to express high amounts of human RGR protein in the ARPE-19 human RPE cell line [10].
• Expression of a recombinant human RGR opsin in Lentivirus-transduced cultured cells [10].
• Exon-skipping variant of RGR opsin in human retina and pigment epithelium [11].
• METHODS: A human RGR cDNA was cloned into a replication-defective lentiviral vector, and recombinant hRGR-Lentivirus was prepared for transduction of the ARPE-19, a human retinal pigment epithelium (RPE) cell line, and COS-7 cells [10].

Associations of CRSP2 with chemical compounds

• Coactivation of ERalpha by DRIP150 in ZR-75 cells was activation function 2-dependent and required an intact helix 12 that typically interacts with LXXLL motifs (NR box) in p160 steroid receptor coactivators [1].

Other interactions of CRSP2

• DRIP150 coactivation of estrogen receptor alpha in ZR-75 breast cancer cells is independent of LXXLL motifs [1].
• CRSP-2 has been identified in the pig and dog, and CRSP-3 has been identified only in the pig [12].

References